4CLL3_ORYSJ
ID 4CLL3_ORYSJ Reviewed; 591 AA.
AC Q6YYZ2; C7J6B0;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=4-coumarate--CoA ligase-like 3;
DE EC=6.2.1.-;
GN Name=4CLL3; OrderedLocusNames=Os08g0143300, LOC_Os08g04770;
GN ORFNames=P0025F03.16, P0473D02.38;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP GENE FAMILY.
RX PubMed=18627494; DOI=10.1111/j.1469-8137.2008.02534.x;
RA de Azevedo Souza C., Barbazuk B., Ralph S.G., Bohlmann J., Hamberger B.,
RA Douglas C.J.;
RT "Genome-wide analysis of a land plant-specific acyl:coenzyme A synthetase
RT (ACS) gene family in Arabidopsis, poplar, rice and Physcomitrella.";
RL New Phytol. 179:987-1003(2008).
CC -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in
CC the substrate recognition, and are sufficient to confer the substrate
CC specificity.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AP004381; BAD17022.1; -; Genomic_DNA.
DR EMBL; AP005542; BAD13196.1; -; Genomic_DNA.
DR EMBL; AP008214; BAH94104.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT03799.1; -; Genomic_DNA.
DR RefSeq; XP_015650198.1; XM_015794712.1.
DR AlphaFoldDB; Q6YYZ2; -.
DR SMR; Q6YYZ2; -.
DR STRING; 4530.OS08T0143300-00; -.
DR PaxDb; Q6YYZ2; -.
DR PRIDE; Q6YYZ2; -.
DR EnsemblPlants; Os08t0143300-00; Os08t0143300-00; Os08g0143300.
DR GeneID; 9269113; -.
DR Gramene; Os08t0143300-00; Os08t0143300-00; Os08g0143300.
DR KEGG; osa:9269113; -.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_2_1; -.
DR InParanoid; Q6YYZ2; -.
DR OMA; RVAAYKY; -.
DR OrthoDB; 683933at2759; -.
DR PlantReactome; R-OSA-1119316; Phenylpropanoid biosynthesis.
DR PlantReactome; R-OSA-1119531; Flavonoid biosynthesis.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q6YYZ2; OS.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0106290; F:trans-cinnamate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProt.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..591
FT /note="4-coumarate--CoA ligase-like 3"
FT /id="PRO_0000351629"
FT REGION 303..375
FT /note="SBD1"
FT REGION 376..440
FT /note="SBD2"
FT BINDING 228..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 376..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 459
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 591 AA; 62081 MW; B128A79F1B0934C1 CRC64;
MQRDAIAAAR NAGCSSGRIS QPPPPPFYSA ATGIYSSIHP PVALPTDPSL TLVAHLFARL
PLADPGAPTL VDAATASAVS RADLRRLVAS LAAGLRRRHG VRKGSVVLLL LPNSVAFPVS
FLAVLAAGAV ATTMNPSSSP AEIAAQARAT GACLVLASRD GAARLPPLAA PVVLVPEILD
HSAAADDGDD DQRVFAAFRA MLDGGGGDGT ETAVPVVGQD DAVAILYSSG TSGRSKGVVL
THRNLIAMTE LFVRFEASQY HARGARENVY MAALPMSHVY GLSLFAVGLL SIGATVVVMR
RFDAGDAVAA IGRYKVTHMP LVPPIMAAMV RAAAAGGVPP SQVASLVQVS CGAAPITAAL
IHEFLQAFPH VDFIQGYGMT ESTAVGTRGF NTSKHKKYTS VGLLAPNMHA KIVHLESSSC
LPPGFSGELW LHGPGIMKGY LSDDDDACTR KDGWLRTGDI AYFDLDGYLY IVGRLKDTIK
YKGFQIAPGD LEEVLIHHPE ILDVAVTSAE DEEAGEIPVA FVVRRSGSNL SCKQVMEYVA
KQVAPYKRVR KVVFVEAIPK SPAGKVLRRL LRNSHDTAAA ATSSCSISSK L
